Research workbench
Crystal structure of Q24A Q25A mutant of human macrophage migration inhibitory factor
Analyse Crystal structure of Q24A Q25A mutant of human macrophage migration inhibitory… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TRU
- Type
- protein
- Length
- 342 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Macrophage migration inhibitory factor
- EC
- 5.3.2.1, 5.3.3.12
- UniProt
- P14174
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Macrophage migration inhibitory factor (EC 5.3.2.1, 5.3.3.12) | protein | 114 | 38% helix, 31% strand | P14174 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
- IPA · Isopropyl alcohol · additive · 3 copies · chains A, B, C
- GOL · Glycerol · additive · 2 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 388 | 0.83 | 0.91 | 47 | empty |
| 2 | 61 | 0.54 | 0.87 | 13 | GOL |
| 3 | 58 | 0.48 | 0.84 | 12 | empty |
| 4 | 66 | 0.45 | 0.82 | 13 | GOL |
| 5 | 128 | 0.38 | 0.73 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1109 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1105 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1094 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 4TRU · Crystal structure of Q24A Q25A mutant of human macrophage migration inhibitory factor · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P14174
- Elsewhere: RCSB PDB 4TRU · PDBe 4TRU · UniProt P14174
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